ID G7GJR1_9ACTN Unreviewed; 642 AA.
AC G7GJR1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN Name=sirA {ECO:0000313|EMBL:GAB03836.1};
GN ORFNames=GOAMR_06_00420 {ECO:0000313|EMBL:GAB03836.1};
OS Gordonia amarae NBRC 15530.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB03836.1, ECO:0000313|Proteomes:UP000006023};
RN [1] {ECO:0000313|EMBL:GAB03836.1, ECO:0000313|Proteomes:UP000006023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB03836.1,
RC ECO:0000313|Proteomes:UP000006023};
RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000256|ARBA:ARBA00003247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB03836.1}.
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DR EMBL; BAED01000006; GAB03836.1; -; Genomic_DNA.
DR RefSeq; WP_005182098.1; NZ_BAED01000006.1.
DR AlphaFoldDB; G7GJR1; -.
DR STRING; 1075090.GOAMR_06_00420; -.
DR eggNOG; COG0155; Bacteria.
DR Proteomes; UP000006023; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006023};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 178..240
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 248..402
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 425..486
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 498..641
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 71125 MW; CB3CEF86416860C5 CRC64;
MTSTTDALTA SDSPEPADGT PADAGSASDT AAAGTRPRTR PRAPRTAANG DTPVRQRTPR
TPAADGEAAP RTRTPRAPRA AADGDAPARK PRPVKRRAEG QWKLGYREPL NPNEQVKKDD
HPLNVRARIE NIYAKNGFDS IDKQDLRGRM RWWGLYTQRR EGYDGTFTGD ENIDLLEDSH
FMMRIRCDGG ALSAEQLRTL GQLSTEFARD TADLSDRENV QYHWIRIEDV PTIWERIEAV
GLKTTQACGD CPRVVLGSPL AGEAVDEVLD PTPAIDEIVR RYIGDKNLSN LPRKFKTAIS
GLQDVAHEIN DVAFIGVVHP EHGPGLDLWV GGGLSTNPML AQRVGAWIPL DEVPDVWEAV
VSIFRDYGYR RLRSKARLKF LIKDWGIEKF RQVLEDEYLG RKLIDGPAPE PLKAPRDHVG
VQKLKNGLNA VGFAAIAGRV SGTKLTAIAD AAERVGSDRI RFTPYQKLIV LDVPDDKVDE
LVDELATHGL SGRPSNWRRN LMACSGIEFC KLSFVETRKR SQDLVPELEQ RLADINDKLD
VPITVNINGC PNSCARSQIA DIGFKGQLVE DDNGGQTEGF QVHLGGSLGL DSGFGRKLRQ
HKVTSAEMGD YVDRVVRNFI EQREEGERFA QWAVRADEEA LR
//
